Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA

Sebastian Leidel, Patrick G. A. Pedrioli, Tamara Bucher, Renée Brost, Michael Costanzo, Alexander Schmidt, Ruedi Aebersold, Charles Boone, Kay Hofmann () and Matthias Peter ()
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Sebastian Leidel: Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland
Patrick G. A. Pedrioli: Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland
Tamara Bucher: Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland
Renée Brost: University of Toronto, Toronto, Ontario M5S 3E1, Canada
Michael Costanzo: University of Toronto, Toronto, Ontario M5S 3E1, Canada
Alexander Schmidt: Institute of Molecular Systems Biology, ETH Zurich, Wolfgang-Pauli-Strasse 16, CH-8093 Zurich, Switzerland
Ruedi Aebersold: Institute of Molecular Systems Biology, ETH Zurich, Wolfgang-Pauli-Strasse 16, CH-8093 Zurich, Switzerland
Charles Boone: University of Toronto, Toronto, Ontario M5S 3E1, Canada
Kay Hofmann: Bioinformatics Group, Miltenyi Biotec GmbH, Friedrich-Ebert-Strasse 68, 51429 Bergisch-Gladbach, Germany
Matthias Peter: Institute of Biochemistry, ETH Zurich, Schafmattstrasse 18, CH-8093 Zurich, Switzerland

Nature, 2009, vol. 458, issue 7235, 228-232

Abstract: Evolution of ubiquitin-like systems Covalent attachment of ubiquitin-like proteins (UBLs) can modify a protein's function or localization. In bacteria, UBL homologues act as sulphur carriers. Leidel et al. now show that the oldest UBL protein, Urm1p from yeast, is also a sulphur carrier that modifies transfer RNA. Urm1p is first adenylated by, and then thiolated by, Uba4p, after which the sulphur moiety is transferred to the U34 'wobble' position in cytoplasmic adenylated tRNAs. This finding adds support for the theory that ubiquitin-like systems evolved from bacterial sulphur-carrier systems. The identification of a pathway generating thiolated uridine at the tRNA wobble position might also have therapeutic implications, since HIV reverse transcriptase relies on this modification to initiate reverse transcription of the HIV RNA-genome in vitro.

Date: 2009
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DOI: 10.1038/nature07643

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